Adsorption and immobilization of cytochrome c on nanodiamonds

Methods have been developed to immobilize proteins onto the surfaces ofnanodiamonds with an average size of 5 +/- 1 nm. The immobilization started with carboxylation/oxidization of diamonds with strong acids, followed by coating the surfaces with poly-L-lysine (PL) for covalent attachment of protein...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 14 vom: 06. Juli, Seite 5879-84
1. Verfasser: Huang, L C Lora (VerfasserIn)
Weitere Verfasser: Chang, Huan-Cheng
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Polylysine 25104-18-1 Diamond 7782-40-3 Cytochromes c 9007-43-6
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520 |a Methods have been developed to immobilize proteins onto the surfaces ofnanodiamonds with an average size of 5 +/- 1 nm. The immobilization started with carboxylation/oxidization of diamonds with strong acids, followed by coating the surfaces with poly-L-lysine (PL) for covalent attachment of proteins using heterobifunctional cross-linkers. The feasibility of this approach is proven with fluorescent labeling of the PL-coated diamonds by Alexa Fluor 488 and subsequent detection of the emission using a confocal fluorescence microscope. Immobilization of proteins onto the surfaces is also demonstrated with yeast cytochrome c, which possesses a free SH group for linkage and a characteristic Soret absorption band for observation 
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